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Protein

Unconventional myosin-X

Gene

MYO10

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.By similarity9 Publications

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-10 (MYH10).Curated
Originally predicted to contain a coiled coil domain but shown to contain a stable SAH domain instead.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi157 – 164ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • actin-dependent ATPase activity Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: UniProtKB-KW
  • microtubule binding Source: InterPro
  • microtubule motor activity Source: InterPro
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  • plus-end directed microfilament motor activity Source: UniProtKB

GO - Biological processi

  • cytoskeleton-dependent intracellular transport Source: UniProtKB
  • microtubule-based movement Source: InterPro
  • regulation of cell shape Source: UniProtKB
  • regulation of filopodium assembly Source: UniProtKB
  • signal transduction Source: InterPro

Keywordsi

Molecular functionActin-binding, Calmodulin-binding, Motor protein, Myosin
Biological processTransport
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-X
Alternative name(s):
Unconventional myosin-10
Gene namesi
Name:MYO10
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001234721 – 2052Unconventional myosin-XAdd BLAST2052

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei963PhosphoserineBy similarity1
Modified residuei966PhosphoserineBy similarity1
Modified residuei1152PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP79114
PRIDEiP79114

Expressioni

Tissue specificityi

Detected in kidney, testis, liver, kidney, cerebellum and brain cortex (at protein level).1 Publication

Interactioni

Subunit structurei

Monomer, when in an inactive confomation in the cytosol. Homodimer in its active, membrane-bound conformation; antiparallel coiled coil-mediated dimer formation. Interacts with ECPAS. Interacts with NEO 1. Interacts with VASP. Interacts with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding. Interacts strongly with CALM3 and weakly with CALM, the CALM3 interaction is essential for function in filopodial extension and motility (By similarity). Interacts with ITGB1, ITGB3 and ITGB5.By similarity4 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB-KW
  • microtubule binding Source: InterPro

Protein-protein interaction databases

DIPiDIP-46150N
IntActiP79114, 8 interactors
STRINGi9913.ENSBTAP00000026812

Structurei

Secondary structure

12052
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi801 – 861Combined sources61
Helixi864 – 872Combined sources9
Turni873 – 878Combined sources6
Helixi879 – 910Combined sources32
Helixi914 – 925Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N9BNMR-A/B884-921[»]
5HMOX-ray3.49A/C796-929[»]
ProteinModelPortaliP79114
SMRiP79114
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 739Myosin motorPROSITE-ProRule annotationAdd BLAST677
Domaini742 – 763IQ 1PROSITE-ProRule annotationAdd BLAST22
Domaini764 – 787IQ 2PROSITE-ProRule annotationAdd BLAST24
Domaini788 – 817IQ 3PROSITE-ProRule annotationAdd BLAST30
Domaini1206 – 1304PH 1PROSITE-ProRule annotationAdd BLAST99
Domaini1386 – 1491PH 2PROSITE-ProRule annotationAdd BLAST106
Domaini1541 – 1689MyTH4PROSITE-ProRule annotationAdd BLAST149
Domaini1694 – 2038FERMPROSITE-ProRule annotationAdd BLAST345

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni619 – 641Actin-bindingPROSITE-ProRule annotationAdd BLAST23
Regioni815 – 909SAH1 PublicationAdd BLAST95
Regioni884 – 934Mediates antiparallel dimerizationBy similarityAdd BLAST51

Domaini

Interaction between the motor domain and the tail leads to an inactive, monomeric conformation. Phospholipid binding via the PH domains leads to the formation of the active, dimeric form of the protein and strongly increases actin-dependent ATPase activity and motor activity.
Interacts with membranes containing phosphatidylinositol-3,4,5-trisphosphate via the PH domains.
IQ 3 domain mediates high-affinity calcium-dependent binding to CALM3/CLP.By similarity
The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. It can refold after extension suggesting an in vivo force-dependent function. The isolated SAH domain is monomeric; however, in its distal part seems to form a semirigid helical structure which overlaps with a region shown to mediate antiparallel coiled coil-mediated dimerization (PubMed:25122759).1 Publication

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4229 Eukaryota
COG5022 LUCA
HOGENOMiHOG000007044
HOVERGENiHBG052553
InParanoidiP79114
KOiK12559

Family and domain databases

CDDicd14473 FERM_B-lobe, 1 hit
cd14873 MYSc_Myo10, 1 hit
Gene3Di1.20.80.10, 1 hit
1.25.40.530, 1 hit
2.30.29.30, 5 hits
3.40.850.10, 3 hits
InterProiView protein in InterPro
IPR019749 Band_41_domain
IPR014352 FERM/acyl-CoA-bd_prot_sf
IPR035963 FERM_2
IPR019748 FERM_central
IPR000299 FERM_domain
IPR000048 IQ_motif_EF-hand-BS
IPR036961 Kinesin_motor_dom_sf
IPR031971 MYO10_CC
IPR001609 Myosin_head_motor_dom
IPR036124 MYSc_Myo10
IPR000857 MyTH4_dom
IPR038185 MyTH4_dom_sf
IPR027417 P-loop_NTPase
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR000159 RA_dom
PfamiView protein in Pfam
PF00373 FERM_M, 1 hit
PF00612 IQ, 3 hits
PF16735 MYO10_CC, 1 hit
PF00063 Myosin_head, 1 hit
PF00784 MyTH4, 1 hit
PF00169 PH, 2 hits
PF00788 RA, 1 hit
PRINTSiPR00193 MYOSINHEAVY
SMARTiView protein in SMART
SM00295 B41, 1 hit
SM00015 IQ, 3 hits
SM00242 MYSc, 1 hit
SM00139 MyTH4, 1 hit
SM00233 PH, 2 hits
SUPFAMiSSF47031 SSF47031, 2 hits
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS50057 FERM_3, 1 hit
PS50096 IQ, 2 hits
PS51456 MYOSIN_MOTOR, 1 hit
PS51016 MYTH4, 1 hit
PS50003 PH_DOMAIN, 2 hits

Sequencei

Sequence statusi: Complete.

P79114-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNFFPEGTR VWLRENGQHF PSTVNSCAEG VVVFQTDYGQ VFTYKQSTIT
60 70 80 90 100
HQKVMPMQPT DEEGVDDMAT LTELHGGAIM HNLYQRYKRN QIYTYIGSII
110 120 130 140 150
ASVNPYKTIT GLYSRDAVDR YSRCHLGELP PHVFAIANEC YRCLWKRHDN
160 170 180 190 200
QCVLISGESG AGKTESTKLI LKFLSAISQQ SVDLSSKEKT SSVEQAILES
210 220 230 240 250
SPIMEAFGNA KTVYNNNSSR FGKFVQLNIG QKGNIQGGRI VDYLLEKNRV
260 270 280 290 300
VRQNPGERNY HIFYALLAGL GHEEREEFYL SVPENYHYLN QSGCVTDRTI
310 320 330 340 350
SDQESFREVI MAMEVMQFSK EEVREVLRLL AGILHLGNIE FITAGGAQVS
360 370 380 390 400
FKTALGRSAE LLGLDPAQLT DALTQRSMFL RGEEILTPLN VQQAADSRDS
410 420 430 440 450
LAMALYARCF EWVIKKINSR IKGKDDFKSI GILDIFGFEN FEVNHFEQFN
460 470 480 490 500
INYANEKLQE YFNKHIFSLE QLEYSREGLV WEDIDWIDNG ECLDLIEKKL
510 520 530 540 550
GLLALINEES HFPQATDSTL LEKLHNQHAN NHFYVKPRVA VNNFGVKHYA
560 570 580 590 600
GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH VSSRNNQDTL
610 620 630 640 650
KCGSKHRRPT VSSQFKDSLH SLMATLSASN PFFVRCIKPN MQKMPDQFDQ
660 670 680 690 700
AVVVNQLRYS GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RNVALPEDIR
710 720 730 740 750
GKCTALLQLY DASNSEWQLG KTKVFLRESL EQKLEKRQEE EVTRAAMVIR
760 770 780 790 800
AHVLGYLARK QYKKVLDCVV IIQKNYRAFL LRRRFLHLKK AAVVFQKQLR
810 820 830 840 850
GQIARRVYRQ LLAEKRAEEE KRKREEEEKR KREEEERERE RERREAELRA
860 870 880 890 900
QQEEAARKQR ELEALQQESQ RAAELSRELE KQKENKQVEE ILRLEKEIED
910 920 930 940 950
LQRMKERQEL SLTEASLQKL QQLRDEELRR LEDEACRAAQ EFLESLNFDE
960 970 980 990 1000
IDECVRNIER SLSVGSGCTG EQGAGAEKPS FNFSQPYPEE EEVDEGFEAD
1010 1020 1030 1040 1050
DDAFKDSPNP SEHGHSDQRT SGIRTSDESS EEDPYMNDTV VPTSPSADST
1060 1070 1080 1090 1100
VLLAPSEHDS SAGEPTYCLP QTPGALPAPE GDYDYDQDDY EDGAITSGSS
1110 1120 1130 1140 1150
VTFSNSCSSQ WSPDYRCSVG TYNSSGAYRF SSEGAQSSFE DSEEDFDSRF
1160 1170 1180 1190 1200
DTDDELSYRR DSVYSCVTLP YFHSFLYMKG GLMNSWKRRW CVLKDETFLW
1210 1220 1230 1240 1250
FRSKQEALKQ GWLHKKGGGS STLSRRNWKK RWFVLRQAKL MYFENDSEEK
1260 1270 1280 1290 1300
LKGTVEVRAA KEIIDNTSKE NGIDIIMADR TFHLIAESPE DASQWFSVLS
1310 1320 1330 1340 1350
QVHASTDQEI REMHDEQANP QNAVGTLDVG LIDSVCASDS PDRPNSFVII
1360 1370 1380 1390 1400
TANRVLHCNA DTPEEMHHWI TLLQRSKGDT RVEGQEFIVR GWLHKEVKNS
1410 1420 1430 1440 1450
PKMSSLKLKK RWFVLTHNSL DYYKSSEKNA LKLGTLVLNS LCSVVPPDEK
1460 1470 1480 1490 1500
IFKETGYWNV TVYGRKHCYR LYTKLLNEAT RWSSAIQNVT DTKAPIDTPT
1510 1520 1530 1540 1550
QQLIQDIKEN CLNSDVVEQI YKRNPILRHT HHPLHSPLLP LPYGDINLNL
1560 1570 1580 1590 1600
LKDKGYTTLQ DEAIKIFNSL QQLESMSDPI PIIQGILQTG HDLRPLRDEL
1610 1620 1630 1640 1650
YCQLIKQTNK VPHPGSVGNL CSWQILTCLS CTFLPSRGIL KYLKFHLRRI
1660 1670 1680 1690 1700
REQFPGTEME KYALFIYESL KKTKCREFVP SRDEIEALIH RQEMTSTVHC
1710 1720 1730 1740 1750
HGGGSCKITV NSHTTAGEVV EKLIRGLAME DSRNMFALFE YNGHVDKAIE
1760 1770 1780 1790 1800
SRTIVADVLA KFEKLAATSE VGEQPWKFYF KLYCFLDTDN VPKDSVEFAF
1810 1820 1830 1840 1850
MFEQAHEAVI HGHYPAPEEN LQVLAALRLQ YLQGDYAPHA PVPPLEEVYS
1860 1870 1880 1890 1900
LQRLKARISQ STKSFTPGER LEKRRTSFLE GTLRRSFRTG SAIRQKAEEE
1910 1920 1930 1940 1950
QMVDMWVKEE VCSARASILD KWKKFQGMSQ EQAMAKYMAL IKEWPGYGST
1960 1970 1980 1990 2000
LFDVECKEGG FPQDLWLGVS ADAVSVYKRG EGRPLEVFQY EHILSFGAPL
2010 2020 2030 2040 2050
ANTYKIVVDE RELLFETSEV VDVAKLMKAY ISMIVKKRYS TSRSVSSQGS

SR
Length:2,052
Mass (Da):235,839
Last modified:May 1, 1997 - v1
Checksum:i43DF13424B4B2D28
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55042 mRNA Translation: AAB39486.1
PIRiT18519
RefSeqiNP_776819.1, NM_174394.2
UniGeneiBt.103339

Genome annotation databases

GeneIDi281935
KEGGibta:281935

Similar proteinsi

Entry informationi

Entry nameiMYO10_BOVIN
AccessioniPrimary (citable) accession number: P79114
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: May 1, 1997
Last modified: March 28, 2018
This is version 135 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health